AB9C_ARATH
ID AB9C_ARATH Reviewed; 1506 AA.
AC Q9M1C7; F4JAM7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ABC transporter C family member 9;
DE Short=ABC transporter ABCC.9;
DE Short=AtABCC9;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 9;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 9;
DE AltName: Full=Multidrug resistance-associated protein 9;
GN Name=ABCC9; Synonyms=MRP9; OrderedLocusNames=At3g60160; ORFNames=T2O9.140;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [4]
RP GENE FAMILY.
RX PubMed=11855639; DOI=10.1007/s004250100661;
RA Martinoia E., Klein M., Geisler M., Bovet L., Forestier C.,
RA Kolukisaoglu H.U., Mueller-Roeber B., Schulz B.;
RT "Multifunctionality of plant ABC transporters -- more than just
RT detoxifiers.";
RL Planta 214:345-355(2002).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12430019; DOI=10.1007/s00425-002-0890-6;
RA Kolukisaoglu U.H., Bovet L., Klein M., Eggmann T., Geisler M., Wanke D.,
RA Martinoia E., Schulz B.;
RT "Family business: the multidrug-resistance related protein (MRP) ABC
RT transporter genes in Arabidopsis thaliana.";
RL Planta 216:107-119(2002).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
CC -!- FUNCTION: Pump for glutathione S-conjugates. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12430019}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB75931.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL138658; CAB75931.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80019.1; -; Genomic_DNA.
DR PIR; T47840; T47840.
DR RefSeq; NP_191575.2; NM_115879.7.
DR AlphaFoldDB; Q9M1C7; -.
DR SMR; Q9M1C7; -.
DR STRING; 3702.AT3G60160.1; -.
DR iPTMnet; Q9M1C7; -.
DR PaxDb; Q9M1C7; -.
DR ProteomicsDB; 244633; -.
DR EnsemblPlants; AT3G60160.1; AT3G60160.1; AT3G60160.
DR GeneID; 825186; -.
DR Gramene; AT3G60160.1; AT3G60160.1; AT3G60160.
DR KEGG; ath:AT3G60160; -.
DR Araport; AT3G60160; -.
DR TAIR; locus:2101452; AT3G60160.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_0_1; -.
DR InParanoid; Q9M1C7; -.
DR OrthoDB; 138195at2759; -.
DR BioCyc; ARA:AT3G60160-MON; -.
DR PRO; PR:Q9M1C7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1C7; baseline and differential.
DR Genevisible; Q9M1C7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:TAIR.
DR GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1506
FT /note="ABC transporter C family member 9"
FT /id="PRO_0000226080"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 934..956
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1048..1068
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1167..1187
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1191..1211
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 314..596
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 630..853
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 936..1218
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1257..1489
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 665..672
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1289..1296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1506 AA; 168210 MW; 704CBD1D9EB97DBD CRC64;
MFKPFGFAAE TGSHLLTTQW LQLGNSLCLK ERISIAMQVT FLAFFLIHLA LKWFGVVRNR
GSNDVEEDLK KQSITVKQSF SYNISLLCSV SILGTHCFIL LLLFRDSVVS RCDSSVSVFS
AEVSQSFSWL FVSVVVVKIR ERRLVKFPWM LRSWWLCSFI LSFSFDAHFI TAKHEPLEFQ
DYADLTGLLA SLFLLAVSIR GKTGFHLLES SGNTEPLLLG DQTEQNKKDS YSSSSPYGNA
TLFQRITFSW INPLFSLGYK RPLEKDDVPD IDVKDSARFC SHAFDQKLKT TKEKEGPGNA
FFYNSVLRYV WRKAAINAVF AVVNASTAYI GPYLINDFVE FLSEKQSQSL NHGYLLALGF
LTAKIVETVT QRQWIFGARQ LGLRLRAALI SHIYQKGLVL SSQSRQSHTS GEIINYMSVD
VQRITDFIWY VNNIWMLPIQ IFSAIYILQK HLGLGALAAL VTTLMVMACN YPLTRLQRNY
QSDIMNAKDD RMKATSEILK NMKILKLQAW DNQFLNKVKT LRKKEYDCLW KSLRLQAFTT
FILWGAPSLI SVVTFVTCML MGVKLTAGAV LSALATFQML QSPIFGLPDL LSALVQSKVS
ADRIASYLQQ SETQKDAVEY CSKDHTELSV EIENGAFSWE PESSRPTLDD IELKVKSGMK
VAVCGAVGSG KSSLLSSILG EIQKLKGTVR VSGKQAYVPQ SPWILSGTIR DNILFGSMYE
SEKYERTVKA CALIKDFELF SNGDLTEIGE RGINMSGGQK QRIQIARAVY QNADIYLLDD
PFSAVDAHTG RELFEDCLMG ILKDKTVLYV THQVEFLPAA DLILVMQNGR VMQAGKFEEL
LKQNIGFEVL VGAHNEALDS ILSIEKSSRN FKEGSKDDTA SIAESLQTHC DSEHNISTEN
KKKEAKLVQD EETEKGVIGK EVYLAYLTTV KGGLLVPFII LAQSCFQMLQ IASNYWMAWT
APPTAESIPK LGMGRILLVY ALLAAGSSLC VLARTILVAI GGLSTAETFF SRMLCSIFRA
PMSFFDSTPT GRILNRASTD QSVLDLEMAV KLGWCAFSII QIVGTIFVMS QVAWQVCVIF
IPVAVACVFY QRYYTPTARE LSRMSGVERA PILHHFAESL AGATTIRAFD QRDRFISSNL
VLIDSHSRPW FHVASAMEWL SFRLNLLSHF VFAFSLVLLV TLPEGVINPS IAGLGVTYGL
SLNVLQATVI WNICNAENKM ISVERILQYS KIPSEAPLVI DGHRPLDNWP NVGSIVFRDL
QVRYAEHFPA VLKNITCEFP GGKKIGVVGR TGSGKSTLIQ ALFRIVEPSQ GTIVIDNVDI
TKIGLHDLRS RLGIIPQDPA LFDGTIRLNL DPLAQYTDHE IWEAIDKCQL GDVIRAKDER
LDATVVENGE NWSVGQRQLV CLGRVLLKKS NILVLDEATA SVDSATDGVI QKIINQEFKD
RTVVTIAHRI HTVIESDLVL VLSDGRIAEF DSPAKLLQRE DSFFSKLIKE YSLRSNHFAG
SNDLLS
